ID HAO_NITEU Reviewed; 570 AA. AC Q50925; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Hydroxylamine oxidoreductase; DE Short=HAO; DE EC=1.7.2.6 {ECO:0000269|PubMed:24302732, ECO:0000269|PubMed:497235, ECO:0000269|PubMed:6289867}; DE EC=1.7.2.9 {ECO:0000269|PubMed:497235}; DE Flags: Precursor; GN Name=hao1; OrderedLocusNames=NE2044; GN and GN Name=hao2; OrderedLocusNames=NE0962; GN and GN Name=hao3; OrderedLocusNames=NE2339; OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC OS 14298). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Nitrosomonadaceae; Nitrosomonas. OX NCBI_TaxID=228410; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298; RX PubMed=8288544; DOI=10.1128/jb.176.2.504-510.1994; RA Sayavedra-Soto L.A., Hommes N.G., Arp D.J.; RT "Characterization of the gene encoding hydroxylamine oxidoreductase in RT Nitrosomonas europaea."; RL J. Bacteriol. 176:504-510(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298; RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003; RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.; RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate RT chemolithoautotroph Nitrosomonas europaea."; RL J. Bacteriol. 185:2759-2773(2003). RN [3] RP CATALYTIC ACTIVITY. RX PubMed=497235; DOI=10.1016/0005-2744(79)90220-1; RA Hooper A.B., Terry K.R.; RT "Hydroxylamine oxidoreductase of Nitrosomonas. Production of nitric oxide RT from hydroxylamine."; RL Biochim. Biophys. Acta 571:12-20(1979). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND EPR SPECTROSCOPY. RX PubMed=6289867; DOI=10.1021/bi00260a010; RA Lipscomb J.D., Hooper A.B.; RT "Resolution of multiple heme centers of hydroxylamine oxidoreductase from RT Nitrosomonas. 1. Electron paramagnetic resonance spectroscopy."; RL Biochemistry 21:3965-3972(1982). RN [5] {ECO:0007744|PDB:1FGJ} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-570 IN COMPLEX WITH HEMES C. RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298; RX PubMed=9095195; DOI=10.1038/nsb0497-276; RA Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., Tanaka N.; RT "The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying RT chemoautotrophic bacterium, Nitrosomonas europaea."; RL Nat. Struct. Biol. 4:276-284(1997). RN [6] {ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 25-570 IN COMPLEX WITH RP HYDROXYAMINE AND HEME C, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP SUBUNIT. RX PubMed=24302732; DOI=10.1074/jbc.m113.525147; RA Maalcke W.J., Dietl A., Marritt S.J., Butt J.N., Jetten M.S., RA Keltjens J.T., Barends T.R., Kartal B.; RT "Structural basis of biological NO generation by octaheme RT oxidoreductases."; RL J. Biol. Chem. 289:1228-1242(2014). CC -!- FUNCTION: Catalyzes the oxidation of hydroxylamine to nitrite CC (PubMed:6289867, PubMed:24302732). The electrons released in the CC reaction are partitioned to ammonium monooxygenase and to the CC respiratory chain (PubMed:6289867). The immediate acceptor of electrons CC from HAO is cytochrome c-554 (PubMed:6289867, PubMed:24302732). CC {ECO:0000269|PubMed:24302732, ECO:0000269|PubMed:6289867}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(III)-[cytochrome c] + H2O + hydroxylamine = 4 Fe(II)- CC [cytochrome c] + 5 H(+) + nitrite; Xref=Rhea:RHEA:45032, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:16301, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.6; CC Evidence={ECO:0000269|PubMed:24302732, ECO:0000269|PubMed:497235, CC ECO:0000269|PubMed:6289867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3 Fe(III)-[cytochrome c] + hydroxylamine = 3 Fe(II)- CC [cytochrome c] + 3 H(+) + nitric oxide; Xref=Rhea:RHEA:45036, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15429, ChEBI:CHEBI:16480, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=1.7.2.9; Evidence={ECO:0000269|PubMed:497235}; CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000269|PubMed:24302732, ECO:0000269|PubMed:6289867, CC ECO:0000269|PubMed:9095195}; CC Note=Binds 8 heme c groups per subunit (PubMed:6289867, PubMed:9095195, CC PubMed:24302732). One of them, heme-4, is an atypical heme c (unusual CC heme c binding motif CXXXXCH) and is called P460 (PubMed:6289867, CC PubMed:9095195, PubMed:24302732). Catalysis takes place at heme-4/P460 CC (PubMed:6289867, PubMed:9095195, PubMed:24302732). The other c-type CC hemes mediate electron transfer to the external electron acceptor, CC which is a cytochrome c-type protein (PubMed:6289867, PubMed:9095195, CC PubMed:24302732). {ECO:0000269|PubMed:24302732, CC ECO:0000269|PubMed:6289867, ECO:0000269|PubMed:9095195}; CC -!- SUBUNIT: Homotrimer; subunits are linked by two covalent bonds between CC Tyr-491 of one subunit and heme P460 of an adjacent subunit. CC {ECO:0000269|PubMed:24302732}. CC -!- SUBCELLULAR LOCATION: Anammoxosome {ECO:0000250|UniProtKB:Q1PX48}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U04053; AAC43216.1; -; Unassigned_DNA. DR EMBL; AL954747; CAD84873.1; -; Genomic_DNA. DR EMBL; AL954747; CAD85955.1; -; Genomic_DNA. DR EMBL; AL954747; CAD86251.1; -; Genomic_DNA. DR PIR; A36954; A36954. DR PDB; 1FGJ; X-ray; 2.80 A; A/B=25-570. DR PDB; 4FAS; X-ray; 2.10 A; A/B/C=25-570. DR PDB; 4N4N; X-ray; 2.20 A; A/C/E=25-570. DR PDB; 4N4O; X-ray; 2.47 A; A/C/E=25-570. DR PDB; 6M0P; X-ray; 2.78 A; A/C/E=1-570. DR PDB; 6M0Q; X-ray; 1.99 A; A/C/E/G/I/K=1-570. DR PDBsum; 1FGJ; -. DR PDBsum; 4FAS; -. DR PDBsum; 4N4N; -. DR PDBsum; 4N4O; -. DR PDBsum; 6M0P; -. DR PDBsum; 6M0Q; -. DR AlphaFoldDB; Q50925; -. DR SMR; Q50925; -. DR STRING; 228410.NE0962; -. DR KEGG; neu:NE0962; -. DR KEGG; neu:NE2044; -. DR KEGG; neu:NE2339; -. DR eggNOG; COG3303; Bacteria. DR HOGENOM; CLU_022756_0_0_4; -. DR OrthoDB; 9814800at2; -. DR BioCyc; MetaCyc:HAONITRO-MONOMER; -. DR BRENDA; 1.7.2.6; 3654. DR EvolutionaryTrace; Q50925; -. DR Proteomes; UP000001416; Chromosome. DR GO; GO:0044222; C:anammoxosome; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0047991; F:hydroxylamine oxidase activity; IDA:CACAO. DR GO; GO:0033740; F:hydroxylamine oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IDA:CACAO. DR GO; GO:0019331; P:anaerobic respiration, using ammonium as electron donor; IDA:CACAO. DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB. DR InterPro; IPR012138; HAO. DR InterPro; IPR036280; Multihaem_cyt_sf. DR Pfam; PF13447; Multi-haem_cyto; 1. DR PIRSF; PIRSF000242; HAO; 1. DR SUPFAM; SSF48695; Multiheme cytochromes; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Signal. FT SIGNAL 1..24 FT CHAIN 25..570 FT /note="Hydroxylamine oxidoreductase" FT /evidence="ECO:0000269|PubMed:8288544" FT /id="PRO_0000006604" FT BINDING 103 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 106 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 107 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 123 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 169 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 172 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 173 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 184 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 196 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 199 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 200 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 228 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 253 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 256 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 257 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 263 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 266 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 267 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 270 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 283 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 286 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 287 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 292 FT /ligand="hydroxylamine" FT /ligand_id="ChEBI:CHEBI:15429" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0007744|PDB:4N4O" FT BINDING 303 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 334 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 337 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 338 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 347 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 384 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 387 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 388 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 483 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000269|PubMed:24302732, FT ECO:0000269|PubMed:9095195, ECO:0007744|PDB:1FGJ, FT ECO:0007744|PDB:4N4N, ECO:0007744|PDB:4N4O" FT BINDING 491 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent; ligand shared between tetrameric partners" FT /evidence="ECO:0000269|PubMed:24302732" FT CONFLICT 243 FT /note="A -> T (in Ref. 1; AAC43216)" FT /evidence="ECO:0000305" FT CONFLICT 470 FT /note="A -> G (in Ref. 1; AAC43216)" FT /evidence="ECO:0000305" FT HELIX 31..36 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 41..43 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 112..120 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 140..154 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 193..199 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 201..208 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 210..213 FT /evidence="ECO:0007829|PDB:6M0Q" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 231..236 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 239..243 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 247..255 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 259..261 FT /evidence="ECO:0007829|PDB:6M0Q" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 269..271 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 274..277 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:6M0Q" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:6M0P" FT HELIX 294..300 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 302..310 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 320..322 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 323..327 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 334..338 FT /evidence="ECO:0007829|PDB:6M0Q" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 362..365 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 366..369 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 371..384 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 385..387 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 390..424 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 428..432 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 448..451 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 461..471 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 473..482 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:6M0Q" FT TURN 489..491 FT /evidence="ECO:0007829|PDB:6M0Q" FT STRAND 492..494 FT /evidence="ECO:0007829|PDB:6M0Q" FT HELIX 495..526 FT /evidence="ECO:0007829|PDB:6M0Q" SQ SEQUENCE 570 AA; 64259 MW; C76AB9019512105E CRC64; MRIGEWMRGL LLCAGLMMCG VVHADISTVP DETYDALKLD RGKATPKETY EALVKRYKDP AHGAGKGTMG DYWEPIAISI YMDPNTFYKP PVSPKEVAER KDCVECHSDE TPVWVRAWKR STHANLDKIR NLKSDDPLYY KKGKLEEVEN NLRSMGKLGE KETLKEVGCI DCHVDVNKKD KADHTKDIRM PTADTCGTCH LREFAERESE RDTMVWPNGQ WPAGRPSHAL DYTANIETTV WAAMPQREVA EGCTMCHTNQ NKCDNCHTRH EFSAAESRKP EACATCHSGV DHNNWEAYTM SKHGKLAEMN RDKWNWEVRL KDAFSKGGQN APTCAACHME YEGEYTHNIT RKTRWANYPF VPGIAENITS DWSEARLDSW VLTCTQCHSE RFARSYLDLM DKGTLEGLAK YQEANAIVHK MYEDGTLTGQ KTNRPNPPEP EKPGFGIFTQ LFWSKGNNPA SLELKVLEMA ENNLAKMHVG LAHVNPGGWT YTEGWGPMNR AYVEIQDEYT KMQELSALQA RVNKLEGKQT SLLDLKGTGE KISLGGLGGG MLLAGALALI GWRKRKQTRA //